Nucleus-specific linker histones Hho1 and Mlh1 form distinct protein interactions during growth, starvation and development in Tetrahymena thermophila.
Amino Acid Sequence
Animals
Cell Nucleus
/ genetics
Chromatin
/ genetics
Gene Expression Regulation
Gene Expression Regulation, Developmental
High Mobility Group Proteins
/ genetics
Histones
/ metabolism
MutL Protein Homolog 1
/ genetics
Protein Interaction Domains and Motifs
Proteome
/ analysis
Protozoan Proteins
/ genetics
Starvation
Tetrahymena thermophila
/ genetics
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
13 01 2020
13 01 2020
Historique:
received:
19
07
2019
accepted:
14
11
2019
entrez:
15
1
2020
pubmed:
15
1
2020
medline:
13
11
2020
Statut:
epublish
Résumé
Chromatin organization influences most aspects of gene expression regulation. The linker histone H1, along with the core histones, is a key component of eukaryotic chromatin. Despite its critical roles in chromatin structure and function and gene regulation, studies regarding the H1 protein-protein interaction networks, particularly outside of Opisthokonts, are limited. The nuclear dimorphic ciliate protozoan Tetrahymena thermophila encodes two distinct nucleus-specific linker histones, macronuclear Hho1 and micronuclear Mlh1. We used a comparative proteomics approach to identify the Hho1 and Mlh1 protein-protein interaction networks in Tetrahymena during growth, starvation, and sexual development. Affinity purification followed by mass spectrometry analysis of the Hho1 and Mlh1 proteins revealed a non-overlapping set of co-purifying proteins suggesting that Tetrahymena nucleus-specific linker histones are subject to distinct regulatory pathways. Furthermore, we found that linker histones interact with distinct proteins under the different stages of the Tetrahymena life cycle. Hho1 and Mlh1 co-purified with several Tetrahymena-specific as well as conserved interacting partners involved in chromatin structure and function and other important cellular pathways. Our results suggest that nucleus-specific linker histones might be subject to nucleus-specific regulatory pathways and are dynamically regulated under different stages of the Tetrahymena life cycle.
Identifiants
pubmed: 31932604
doi: 10.1038/s41598-019-56867-0
pii: 10.1038/s41598-019-56867-0
pmc: PMC6957481
doi:
Substances chimiques
Chromatin
0
High Mobility Group Proteins
0
Histones
0
Proteome
0
Protozoan Proteins
0
MutL Protein Homolog 1
EC 3.6.1.3
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
168Références
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